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X-linked ichthyosis

X-linked ichthyosis is an inborn error of metabolism characterized by a deficiency in microsomal sulfatase. It is also referred to as placental sulfatase deficiency. more...

X-linked adrenal...
X-linked ichthyosis
X-linked severe combined...
Xeroderma pigmentosum
XX male syndrome
XY Female

The genetic locus for the steroid sulfatase gene has been mapped to the distal short arm of the x chromosome (Xp22.32). Affected individuals, usually male, develop ichthyosis in the form of hyperkeratosis after birth, sometimes associated with pyloric stenosis, cryptorchism, or cornual opacities.

Prenatally, the condition affects placental estrogen production, as precursor steroids from the male fetus are not fully utilized due to difficulty in removing their sulfate group. Estriol levels during pregnancy are low. Pregnancies may be complicated by an inability to go into spontaneous labor. Typically children are delivered by cesarean section.


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Stratum corneum protein dynamics as evaluated by a spin-label maleimide derivative: Effect of urea
From Biophysical Journal, 12/1/01 by Alonso, Antonio

ABSTRACT The stratum corneum (SC) protein dynamics in the sulfhydryl group regions was studied by electron paramagnetic resonance (EPR) spectroscopy of a covalently attached maleimide derivative spin label. A two-state model for the nitroxide described the coexistence of two spectral components in the EPR spectra. The so-called strongly immobilized component arises from a spin-label fraction with the nitroxide moiety hydrogen-bonded to protein (rigid structure) and the weakly immobilized component is provided by the spin labels with higher mobility (~10 times greater) exposed to the aqueous environment. The relative populations between these two states are in thermodynamic equilibrium. The apparent energetic gain for the nitroxide to form a hydrogen bond with the backbone rather than to be dissolved in the local environment was ~10 kcal/mol in the temperature range of 2-30 deg C and ~6 kcal/mol in the range of 30-70'C. Urea treatment caused a drastic increase in the segmental motion of the polypeptide chains that was completely reversible by its removal. Our analyses also indicated that the urea induced unfolding of the SC proteins opening the thiol group cavities. This work can also be useful to improve the spectral analysis of site-directed spin-labeling, especially for a more quantitative description of the nitroxide side chain mobility.


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Antonio Alonso,* Wilmar Pereira dos Santos,* Sergio Jacintho Leonor,* Judes Gongalves dos Santos,* and Marcel Tabak^

*Instituto de Fisica, Universidade Federal de Goias, Goiania 74001-970, Brazil; and tlnstituto de Quimica de Sao Carlos, Universidade de Sao Paulo, Sao Carlos 13560-970, Brazil

Received fro publication 12 January 2001 and in final form 23 August 2001.

Address reprint requests to Dr. Antonio Alonso, Universidade Federal de Goias, Goiania 74001-970, Brazil. Tel 55-62-521-1470; Fax 55-62-521-- 1014: E-mail:

(C) 2001 by the Biophysical Society

0006-3495/01/12/3566/11 $2.00

We thank Prof. Dr. Fernando Pelegrini (Instituto de Fisica, Universidade Federal de Goias) for his interest in this work. We thank Professors Richard H. Crepeau, Keith A. Earle, and Mingtao Ge for helping us to install the program NLLS.

This work was supported by Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq; grant process 300908/92-0), Fundaqao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP; processes 97/ 02431-4 and 95/6177-0), and Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES).

Copyright Biophysical Society Dec 2001
Provided by ProQuest Information and Learning Company. All rights Reserved

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